A Quantitative Proteomic Analysis of Brassinosteroid-induced Protein Phosphorylation in Rice (Oryza sativa L.)

Hou, Yuxuan; Qiu, Jian; Wang, Yifeng; Li, Zhiyong; Zhao, Juan; Tong, Xiaohong; Lin, Haiyan; Zhang, Jian

doi:10.3389/fpls.2017.00514

Cited by 25 publications

(20 citation statements)

References 81 publications

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“…Quantitative RT-PCR was performed as described by Hou et al (2017) [ 63 ]. Briefly, four micrograms of total RNA was applied for reverse transcription using first strand cDNA synthesis Kit (Toyobo, Shanghai, China).…”

Section: Methodsmentioning

confidence: 99%

Transcriptomic Analysis of Gibberellin- and Paclobutrazol-Treated Rice Seedlings under Submergence

Xiang

Zhang

et al. 2017

IJMS

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Submergence stress is a limiting factor for rice growing in rainfed lowland areas of the world. It is known that the phytohormone gibberellin (GA) has negative effects on submergence tolerance in rice, while its inhibitor paclobutrazol (PB) does the opposite. However, the physiological and molecular basis underlying the GA- and PB-regulated submergence response remains largely unknown. In this study, we reveal that PB could significantly enhance rice seedling survival by retaining a higher level of chlorophyll content and alcohol dehydrogenase activity, and decelerating the consumption of non-structure carbohydrate when compared with the control and GA-treated samples. Further transcriptomic analysis identified 3936 differentially expressed genes (DEGs) among the GA- and PB-treated samples and control, which are extensively involved in the submergence and other abiotic stress responses, phytohormone biosynthesis and signaling, photosynthesis, and nutrient metabolism. The results suggested that PB enhances rice survival under submergence through maintaining the photosynthesis capacity and reducing nutrient metabolism. Taken together, the current study provided new insight into the mechanism of phytohormone-regulated submergence response in rice.

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Section: Methodsmentioning

confidence: 99%

Transcriptomic Analysis of Gibberellin- and Paclobutrazol-Treated Rice Seedlings under Submergence

Xiang

Zhang

et al. 2017

IJMS

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“…Though high-throughput phosphoproteomic studies of plant species other than Arabidopsis are to date uncommon, available studies have found evidence for phosphorylation of the canonical rice Gα, RGA1, at S10 [183] and S110 [173,184–186]. Multiple phosphosites were also identified for an XLG in rice, encoded by the gene Os06t0111400.…”

Section: G Protein Subunit Phosphorylation In Plant Systemsmentioning

confidence: 99%

“…Multiple phosphosites were also identified for an XLG in rice, encoded by the gene Os06t0111400. These rice XLG phosphosites span the protein from the N-terminal domain (S68 [183], S183 [173,183,184], and Y186 [173]) to the Gα-like domain (T669 [184], which is proximal to the G3 motif) to the C-terminal extension that we suggested above to be a potential phosphorylation hotspot (S859/S860/S861 — the exact site could not be conclusively attributed within these three consecutive serines [173]).…”

Section: G Protein Subunit Phosphorylation In Plant Systemsmentioning

confidence: 99%

“…In our own AGB1 immunoprecipitates, Gγs were also present, as expected, and we found evidence consistent with phosphorylation of T5 in AGG1 and of a site(s) among S23/S24/S28/S29 in AGG3 [188] (the phosphosite could not conclusively be attributed within the peptide). Similarly, the rice Gγ subunits RGG2 and DEP1 have been found to be phosphorylated at S38 [184] and S15 [183], respectively. These Gγ phosphosites are reminiscent of the N-terminal sites identified in metazoan Gγs (Figure 4B).…”

Section: G Protein Subunit Phosphorylation In Plant Systemsmentioning

confidence: 99%

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G protein subunit phosphorylation as a regulatory mechanism in heterotrimeric G protein signaling in mammals, yeast, and plants

Chakravorty

Assmann

2018

Biochemical Journal

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Heterotrimeric G proteins composed of Gα, Gβ, and Gγ subunits are vital eukaryotic signaling elements that convey information from ligand-regulated G protein-coupled receptors (GPCRs) to cellular effectors. Heterotrimeric G protein-based signaling pathways are fundamental to human health [Biochimica et Biophysica Acta (2007) 1768, 994–1005] and are the target of >30% of pharmaceuticals in clinical use [Biotechnology Advances (2013) 31, 1676–1694; Nature Reviews Drug Discovery (2017) 16, 829–842]. This review focuses on phosphorylation of G protein subunits as a regulatory mechanism in mammals, budding yeast, and plants. This is a re-emerging field, as evidence for phosphoregulation of mammalian G protein subunits from biochemical studies in the early 1990s can now be complemented with contemporary phosphoproteomics and genetic approaches applied to a diversity of model systems. In addition, new evidence implicates a family of plant kinases, the receptor-like kinases, which are monophyletic with the interleukin-1 receptor-associated kinase/Pelle kinases of metazoans, as possible GPCRs that signal via subunit phosphorylation. We describe early and modern observations on G protein subunit phosphorylation and its functional consequences in these three classes of organisms, and suggest future research directions.

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“…Technological developments in phosphoproteomics now offer novel opportunities to identify phosphosites more globally. Thus, large scale scans of induced phosphoproteins have been carried out with a view to characterizing the plant response to drought [ 22 ], exogenous hormone treatment [ 23 , 24 ], salinity [ 25 ] and high temperature [ 26 ], although not as yet to heavy metal exposure. The current paper presents a comprehensive analysis of phosphorylation induced in rice seedlings by their exposure to Cd, conducted using an iTRAQ (isobaric tag for relative and absolute quantitation) based quantitative phosphoproteomic approach.…”

Section: Introductionmentioning

confidence: 99%

The Phosphoproteomic Response of Rice Seedlings to Cadmium Stress

Zhong

Liu

Huang

et al. 2017

IJMS

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The environmental damage caused by cadmium (Cd) pollution is of increasing concern in China. While the overall plant response to Cd has been investigated in some depth, the contribution (if any) of protein phosphorylation to the detoxification of Cd and the expression of tolerance is uncertain. Here, the molecular basis of the plant response has been explored in hydroponically raised rice seedlings exposed to 10 μΜ and 100 μΜ Cd2+ stress. An analysis of the seedlings’ quantitative phosphoproteome identified 2454 phosphosites, associated with 1244 proteins. A total of 482 of these proteins became differentially phosphorylated as a result of exposure to Cd stress; the number of proteins affected in this way was six times greater in the 100 μΜ Cd2+ treatment than in the 10 μΜ treatment. A functional analysis of the differentially phosphorylated proteins implied that a significant number was involved in signaling, in stress tolerance and in the neutralization of reactive oxygen species, while there was also a marked representation of transcription factors.

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A Quantitative Proteomic Analysis of Brassinosteroid-induced Protein Phosphorylation in Rice (Oryza sativa L.)

Cited by 25 publications

References 81 publications

Transcriptomic Analysis of Gibberellin- and Paclobutrazol-Treated Rice Seedlings under Submergence

Transcriptomic Analysis of Gibberellin- and Paclobutrazol-Treated Rice Seedlings under Submergence

G protein subunit phosphorylation as a regulatory mechanism in heterotrimeric G protein signaling in mammals, yeast, and plants

The Phosphoproteomic Response of Rice Seedlings to Cadmium Stress

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